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1.1.1.71: alcohol dehydrogenase [NAD(P)+]

This is an abbreviated version!
For detailed information about alcohol dehydrogenase [NAD(P)+], go to the full flat file.

Wordmap for 1.1.1.71

Word Map on EC 1.1.1.71 Wordmap for 1.1.1.71

Reaction

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a primary alcohol
+
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NAD(P)+
=
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an aldehyde
 +
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NAD(P)H
 +
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H+

Synonyms

ADH, ADH12, ADH2, Adh319, AdhA, AdhE, alcohol dehydrogenase, aldehyde reductase (NADPH/NADH), DHRS3, HvADH2, HVO_B0071, NAD(P)+-dependent alcohol dehydrogenase, NAD(P)H-dependent ADH, NAD(P)H-dependent aldehyde reductase, NADPH-dependent ADHA, NADPH-dependent alcohol dehydrogenase, PH0743, PhADH, RADH, retinal reductase, retinal short-chain dehydrogenase/reductase member 3, retinaldehyde reductase, Retinol dehydrogenase, retinol-active alcohol dehydrogenase, retSDR1, TeSADH, TsAdh319, Tsib_0319, VNG_2617G, YqhD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                EC 1.1.1.711.1.1.71 alcohol dehydrogenase [NAD(P)+]

Engineering

Engineering on EC 1.1.1.71 - alcohol dehydrogenase [NAD(P)+]

for references in articles please use BRENDA:EC1.1.1.71

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P704L/H734R
the ethanol tolerant phenotype of Clostridium thermocellum is primarily due to a mutated bifunctional acetaldehyde-CoA/alcohol dehydrogenase gene (adhE). The mutant displays a complete loss of NADH-dependent activity with concomitant acquisition of NADPH-dependent activity. The reduction in specific activity with respect to NADH is far greater (about 25fold less activity) than the increase with respect to NADPH. Although total ADH activity dropps by 25fold, ethanol production does not drop significantly between strains under these conditions
D194A
the mutation results in substantial catalytic deficiency (2.8% compared to the wild type enzyme)
H363A
the mutant with full activity is not able to grow on butanal-containing medium
E43K/S97C/T148S/A155H/P210C/L227V/Y244F
-
site-directed mutagenesis, mutant ADHA-0381, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
E43K/S97C/T148S/T194V/M206D/P210C/L227V
-
site-directed mutagenesis, mutant ADHA-0398, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
S97C/M206D
-
site-directed mutagenesis, mutant ADHA-0279, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
S97C/M206D/P210C
-
site-directed mutagenesis, mutant ADHA-0278, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
S97C/T148S/A155H/P210C/L227V
-
site-directed mutagenesis, mutant ADHA-0391, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
S97C/T148S/A155H/P210C/L227V/Y244F
-
site-directed mutagenesis, mutant ADHA-0384, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
E43K/S97C/T148S/T194V/M206D/P210C/L227V
-
site-directed mutagenesis, mutant ADHA-0398, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
-
S97C/M206D
-
site-directed mutagenesis, mutant ADHA-0279, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
-
S97C/M206D/P210C
-
site-directed mutagenesis, mutant ADHA-0278, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
-
S97C/T148S/A155H/P210C/L227V
-
site-directed mutagenesis, mutant ADHA-0391, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
-
G198D
-
site-directed mutagenesis, the variant of the NAD(P)H-dependent ADH, TeSADH, shows a significant switch of cofactor dependence from NADPH towards NADH compared to the wild-type enzyme
W110A
-
site-directed mutagenesis, the mutant is able not only to reduce phenyl-ring-containing ketones with high enantioselectivity, but it can also racemize the corresponding enantiopure alcohols
W110A/I86A
-
site-directed mutagenesis, the mutant of TeSADH reduces phenyl-ring-containing ketones with high enantioselectivity and racemizes the corresponding enantiopure alcohols, and it expands substrate specificity to accommodate ketones bearing two sterically demanding groups
additional information